HEADER APOPTOSIS 17-FEB-19 6O0P
TITLE CRYSTAL STRUCTURE OF BCL-2 G101A MUTATION WITH VENETOCLAX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2,BCL-2-LIKE PROTEIN 1,APOPTOSIS
COMPND 3 REGULATOR BCL-2;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: BCL2-L-1,APOPTOSIS REGULATOR BCL-X;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCL2, BCL2L1, BCL2L, BCLX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: BL21
KEYWDS BCL-2, VENETOCLAX, COMPLEX, PROTEIN-PROTEIN INTERFACE INHIBITOR, FDA
KEYWDS 2 APPROVED DRUG COMPLEX, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.BIRKINSHAW,C.S.LUO,P.M.COLMAN,P.E.CZABOTAR
REVDAT 5 11-DEC-19 6O0P 1 HETSYN
REVDAT 4 20-NOV-19 6O0P 1 COMPND HETNAM FORMUL
REVDAT 3 10-JUL-19 6O0P 1 COMPND SOURCE DBREF SEQADV
REVDAT 2 19-JUN-19 6O0P 1 JRNL
REVDAT 1 22-MAY-19 6O0P 0
JRNL AUTH R.W.BIRKINSHAW,J.N.GONG,C.S.LUO,D.LIO,C.A.WHITE,
JRNL AUTH 2 M.A.ANDERSON,P.BLOMBERY,G.LESSENE,I.J.MAJEWSKI,R.THIJSSEN,
JRNL AUTH 3 A.W.ROBERTS,D.C.S.HUANG,P.M.COLMAN,P.E.CZABOTAR
JRNL TITL STRUCTURES OF BCL-2 IN COMPLEX WITH VENETOCLAX REVEAL THE
JRNL TITL 2 MOLECULAR BASIS OF RESISTANCE MUTATIONS.
JRNL REF NAT COMMUN V. 10 2385 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 31160589
JRNL DOI 10.1038/S41467-019-10363-1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 13525
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 672
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.2495 - 3.0777 1.00 2734 146 0.1736 0.2000
REMARK 3 2 3.0777 - 2.4429 1.00 2614 128 0.1908 0.2554
REMARK 3 3 2.4429 - 2.1341 1.00 2582 143 0.1910 0.2323
REMARK 3 4 2.1341 - 1.9390 1.00 2561 134 0.2325 0.2760
REMARK 3 5 1.9390 - 1.8000 0.92 2362 121 0.3379 0.4271
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 1315
REMARK 3 ANGLE : 0.565 1781
REMARK 3 CHIRALITY : 0.036 172
REMARK 3 PLANARITY : 0.003 262
REMARK 3 DIHEDRAL : 18.382 780
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0667 6.6785 -7.2494
REMARK 3 T TENSOR
REMARK 3 T11: 0.2412 T22: 0.2267
REMARK 3 T33: 0.2070 T12: 0.0037
REMARK 3 T13: -0.0308 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 3.7632 L22: 3.0898
REMARK 3 L33: 5.0092 L12: -1.8535
REMARK 3 L13: -3.3444 L23: 2.4290
REMARK 3 S TENSOR
REMARK 3 S11: 0.1008 S12: -0.1124 S13: 0.2760
REMARK 3 S21: -0.0610 S22: 0.1089 S23: -0.2129
REMARK 3 S31: 0.0141 S32: 0.2325 S33: -0.2520
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7107 -4.5625 -7.8900
REMARK 3 T TENSOR
REMARK 3 T11: 0.2343 T22: 0.2165
REMARK 3 T33: 0.2516 T12: 0.0188
REMARK 3 T13: -0.0341 T23: 0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 4.9918 L22: 6.2293
REMARK 3 L33: 8.3350 L12: 0.5997
REMARK 3 L13: -0.5201 L23: 4.5550
REMARK 3 S TENSOR
REMARK 3 S11: -0.0742 S12: -0.1564 S13: -0.1723
REMARK 3 S21: 0.3847 S22: 0.2294 S23: -0.3631
REMARK 3 S31: 0.3992 S32: 0.2639 S33: -0.1491
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1869 -4.1657 -10.4859
REMARK 3 T TENSOR
REMARK 3 T11: 0.2972 T22: 0.2098
REMARK 3 T33: 0.3733 T12: -0.0363
REMARK 3 T13: 0.0266 T23: -0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 5.4359 L22: 4.7630
REMARK 3 L33: 8.2605 L12: 0.4852
REMARK 3 L13: 0.9617 L23: 1.6705
REMARK 3 S TENSOR
REMARK 3 S11: -0.0697 S12: 0.2069 S13: -0.6276
REMARK 3 S21: -0.1836 S22: 0.1510 S23: 0.0340
REMARK 3 S31: 0.1599 S32: 0.0626 S33: -0.1874
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5657 5.1577 -17.5144
REMARK 3 T TENSOR
REMARK 3 T11: 0.2283 T22: 0.2455
REMARK 3 T33: 0.2349 T12: 0.0124
REMARK 3 T13: -0.0639 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 3.9886 L22: 4.9360
REMARK 3 L33: 4.6631 L12: -2.1779
REMARK 3 L13: -2.8551 L23: 2.4778
REMARK 3 S TENSOR
REMARK 3 S11: 0.2578 S12: 0.3744 S13: 0.1108
REMARK 3 S21: -0.2886 S22: -0.1951 S23: 0.0237
REMARK 3 S31: -0.0407 S32: -0.2287 S33: -0.0822
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6O0P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1000239799.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13559
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 43.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.820
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4LVT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG4K, 40% PEG400, 0.1M MES PH 6.0,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 16.69900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.23700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.47250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.23700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.69900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.47250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 ARG A 6
REMARK 465 THR A 7
REMARK 465 GLY A 8
REMARK 465 VAL A 77
REMARK 465 GLU A 78
REMARK 465 GLU A 79
REMARK 465 ASN A 80
REMARK 465 ARG A 81
REMARK 465 THR A 82
REMARK 465 GLU A 83
REMARK 465 ALA A 84
REMARK 465 PRO A 85
REMARK 465 GLU A 86
REMARK 465 GLY A 87
REMARK 465 THR A 88
REMARK 465 GLU A 89
REMARK 465 PRO A 204
REMARK 465 SER A 205
REMARK 465 MET A 206
REMARK 465 ARG A 207
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 35 CG OD1 OD2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LBM A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 304
DBREF 6O0P A 1 34 UNP P10415 BCL2_HUMAN 1 34
DBREF 6O0P A 35 91 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 6O0P A 92 207 UNP P10415 BCL2_HUMAN 92 207
SEQADV 6O0P ALA A 101 UNP P10415 GLY 101 ENGINEERED MUTATION
SEQRES 1 A 166 MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 A 166 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 A 166 GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU GLU ASN
SEQRES 4 A 166 ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU VAL VAL
SEQRES 5 A 166 HIS LEU THR LEU ARG GLN ALA ALA ASP ASP PHE SER ARG
SEQRES 6 A 166 ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER GLN LEU
SEQRES 7 A 166 HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE ALA THR
SEQRES 8 A 166 VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY
SEQRES 9 A 166 ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL MET CYS
SEQRES 10 A 166 VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU VAL ASP
SEQRES 11 A 166 ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN ARG HIS
SEQRES 12 A 166 LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP ASP ALA
SEQRES 13 A 166 PHE VAL GLU LEU TYR GLY PRO SER MET ARG
HET LBM A 301 61
HET PEG A 302 7
HET PEG A 303 7
HET PEG A 304 7
HETNAM LBM 4-{4-[(4'-CHLORO-5,5-DIMETHYL[3,4,5,6-TETRAHYDRO[1,1'-
HETNAM 2 LBM BIPHENYL]]-2-YL)METHYL]PIPERAZIN-1-YL}-N-[(3-NITRO-4-
HETNAM 3 LBM {[(OXAN-4-YL)METHYL]AMINO}PHENYL)SULFONYL]-2-[(1H-
HETNAM 4 LBM PYRROLO[2,3-B]PYRIDIN-5-YL)OXY]BENZAMIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN LBM VENETOCLAX, 2-((1H-PYRROLO[2,3-B]PYRIDIN-5-YL)OXY)-4-
HETSYN 2 LBM (4-((4'-CHLORO-5,5-DIMETHYL-3,4,5,6-TETRAHYDRO-[1,1'-
HETSYN 3 LBM BIPHENYL]-2-YL)METHYL)PIPERAZIN-1-YL)-N-((3-NITRO-4-
HETSYN 4 LBM (((TETRAHYDRO-2H-PYRAN-4-YL)METHYL)AMINO)PHENYL)
HETSYN 5 LBM SULFONYL)BENZAMIDE
FORMUL 2 LBM C45 H50 CL N7 O7 S
FORMUL 3 PEG 3(C4 H10 O3)
FORMUL 6 HOH *36(H2 O)
HELIX 1 AA1 ASP A 10 ARG A 26 1 17
HELIX 2 AA2 TRP A 30 ASP A 34 5 5
HELIX 3 AA3 GLU A 91 TYR A 108 1 18
HELIX 4 AA4 TYR A 108 LEU A 119 1 12
HELIX 5 AA5 THR A 125 ARG A 139 1 15
HELIX 6 AA6 ASN A 143 ARG A 164 1 22
HELIX 7 AA7 SER A 167 HIS A 184 1 18
HELIX 8 AA8 LEU A 185 ASN A 192 1 8
HELIX 9 AA9 GLY A 193 GLY A 203 1 11
SITE 1 AC1 21 ARG A 12 ALA A 100 ASP A 103 PHE A 104
SITE 2 AC1 21 ARG A 107 TYR A 108 ASP A 111 MET A 115
SITE 3 AC1 21 LEU A 137 ASN A 143 TRP A 144 GLY A 145
SITE 4 AC1 21 VAL A 148 ALA A 149 GLU A 152 PHE A 153
SITE 5 AC1 21 PHE A 198 TYR A 202 HOH A 404 HOH A 408
SITE 6 AC1 21 HOH A 427
SITE 1 AC2 4 ARG A 12 TYR A 108 ASP A 171 PEG A 303
SITE 1 AC3 3 ARG A 12 TYR A 108 PEG A 302
SITE 1 AC4 1 ARG A 107
CRYST1 33.398 48.945 86.474 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.029942 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020431 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011564 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
